ArticlePLoS computational biology2007
Mechanochemical coupling in the myosin motor domain. I. Insights from equilibrium active-site simulations.
Article in PLoS computational biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 55 citations in OpenAlex.
- Mechanoadaptation via Myosin Cytoplasmic Redistribution Protects Circulating Tumor Cells From Shear-induced Death During Hematogenous Dissemination.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- On the Control of Directionality of Myosin.Journal of the American Chemical Society · 2024Article
- A weak coupling mechanism for the early steps of the recovery stroke of myosin VI: A free energy simulation and string method analysis.PLoS computational biology · 2024Article
- Binding pocket dynamics along the recovery stroke of human β-cardiac myosin.PLoS computational biology · 2023Article
- An intermediate along the recovery stroke of myosin VI revealed by X-ray crystallography and molecular dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Analysis of Phosphoryl-Transfer Enzymes with QM/MM Free Energy Simulations.Methods in enzymology · 2018Article
- Allosteric modulation of cardiac myosin dynamics by omecamtiv mecarbil.PLoS computational biology · 2017Article
- Allocating dissipation across a molecular machine cycle to maximize flux.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Regulation and Plasticity of Catalysis in Enzymes: Insights from Analysis of Mechanochemical Coupling in Myosin.Biochemistry · 2017Article
- Highly selective inhibition of myosin motors provides the basis of potential therapeutic application.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Parametrization of DFTB3/3OB for magnesium and zinc for chemical and biological applications.The journal of physical chemistry. B · 2015Article
- Stabilization of the ADP/metaphosphate intermediate during ATP hydrolysis in pre-power stroke myosin: quantitative anatomy of an enzyme.The Journal of biological chemistry · 2013Article
- The mechanism of the converter domain rotation in the recovery stroke of myosin motor protein.Proteins · 2012Article
- Article
- A novel actin binding site of myosin required for effective muscle contraction.Nature structural & molecular biology · 2012Article
- Early stages of the recovery stroke in myosin II studied by molecular dynamics simulations.Protein science : a publication of the Protein Society · 2011Article
- Computational modeling of allosteric communication reveals organizing principles of mutation-induced signaling in ABL and EGFR kinases.PLoS computational biology · 2011Article
- Article
- Atomically detailed simulation of the recovery stroke in myosin by Milestoning.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- The hydrolysis activity of adenosine triphosphate in myosin: a theoretical analysis of anomeric effects and the nature of the transition state.The journal of physical chemistry. A · 2009Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Although the major structural transitions in molecular motors are often argued to couple to the binding of Adenosine triphosphate (ATP), the recovery stroke in the conventional myosin has been shown to be dependent on the hydrolysis of ATP. To obtain a clearer mechanistic picture for such "mechanochemical coupling" in myosin, equilibrium active-site simulations with explicit solvent have been carried out to probe the behavior of the motor domain as functions of the nucleotide chemical state and conformation of the converter/relay helix. In conjunction with previous studies of ATP hydrolysis with different active-site conformations and normal mode analysis of structural flexibility, the results help establish an energetics-based framework for understanding the mechanochemical coupling. It is proposed that the activation of hydrolysis does not require the rotation of the lever arm per se, but the two processes are tightly coordinated because both strongly couple to the open/close transition of the active site. The underlying picture involves shifts in the dominant population of different structural motifs as a consequence of changes elsewhere in the motor domain. The contribution of this work and the accompanying paper [] is to propose the actual mechanism behind these "population shifts" and residues that play important roles in the process. It is suggested that structural flexibilities at both the small and large scales inherent to the motor domain make it possible to implement tight couplings between different structural motifs while maintaining small free-energy drops for processes that occur in the detached states, which is likely a feature shared among many molecular motors. The significantly different flexibility of the active site in different X-ray structures with variable level arm orientations supports the notation that external force sensed by the lever arm may transmit into the active site and influence the chemical steps (nucleotide hydrolysis and/or binding).
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.